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Protein

Ferrichrome outer membrane transporter/phage receptor

Gene

fhuA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the uptake of iron in complex with ferrichrome, an hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane (PubMed:1089064, PubMed:2066336). In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1 (PubMed:1089064, PubMed:353030, PubMed:2066336, PubMed:8617231). The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system (PubMed:353030, PubMed:9353297, PubMed:12427941).6 Publications

Enzyme regulationi

Binding of ferrichrome or colicin M enhances the interaction between FhuA and TonB (PubMed:9353297). TonB activates FhuA through interaction with the beta-barrel (PubMed:12427941).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei114Ferrichrome3 Publications1
Binding sitei133Ferrichrome3 Publications1
Binding sitei424Ferrichrome1 Publication1
Binding sitei735Ferrichrome1 Publication1

GO - Molecular functioni

  • cofactor binding Source: EcoliWiki
  • iron ion binding Source: EcoliWiki
  • protein domain specific binding Source: CAFA
  • receptor activity Source: InterPro
  • toxic substance binding Source: EcoliWiki
  • virion binding Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionReceptor
Biological processIon transport, Iron transport, Transport
LigandIron

Enzyme and pathway databases

BioCyciEcoCyc:EG10302-MONOMER
MetaCyc:EG10302-MONOMER

Protein family/group databases

TCDBi1.B.14.1.2 the outer membrane receptor (omr) family

Names & Taxonomyi

Protein namesi
Recommended name:
Ferrichrome outer membrane transporter/phage receptorCurated
Alternative name(s):
Ferric hydroxamate receptorCurated
Ferric hydroxamate uptakeCurated
Ferrichrome-iron receptor1 Publication
Gene namesi
Name:fhuA1 Publication
Synonyms:tonA1 Publication
Ordered Locus Names:b0150, JW0146
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10302 fhuA

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 192PeriplasmicAdd BLAST159
Transmembranei193 – 201Beta stranded9
Topological domaini202 – 206Extracellular5
Transmembranei207 – 215Beta stranded9
Topological domaini216 – 222Periplasmic7
Transmembranei223 – 231Beta stranded9
Topological domaini232 – 245ExtracellularAdd BLAST14
Transmembranei246 – 255Beta stranded10
Topological domaini256 – 259Periplasmic4
Transmembranei260 – 268Beta stranded9
Topological domaini269 – 312ExtracellularAdd BLAST44
Transmembranei313 – 321Beta stranded9
Topological domaini322 – 326Periplasmic5
Transmembranei327 – 335Beta stranded9
Topological domaini336 – 387ExtracellularAdd BLAST52
Transmembranei388 – 396Beta stranded9
Topological domaini397 – 404Periplasmic8
Transmembranei405 – 413Beta stranded9
Topological domaini414 – 464ExtracellularAdd BLAST51
Transmembranei465 – 473Beta stranded9
Topological domaini474 – 477Periplasmic4
Transmembranei478 – 486Beta stranded9
Topological domaini487 – 508ExtracellularAdd BLAST22
Transmembranei509 – 517Beta stranded9
Topological domaini518 – 522Periplasmic5
Transmembranei523 – 531Beta stranded9
Topological domaini532 – 551ExtracellularAdd BLAST20
Transmembranei552 – 560Beta stranded9
Topological domaini561 – 565Periplasmic5
Transmembranei566 – 574Beta stranded9
Topological domaini575 – 601ExtracellularAdd BLAST27
Transmembranei602 – 610Beta stranded9
Topological domaini611 – 613Periplasmic3
Transmembranei614 – 622Beta stranded9
Topological domaini623 – 645ExtracellularAdd BLAST23
Transmembranei646 – 654Beta stranded9
Topological domaini655 – 661Periplasmic7
Transmembranei662 – 670Beta stranded9
Topological domaini671 – 689ExtracellularAdd BLAST19
Transmembranei690 – 698Beta stranded9
Topological domaini699 – 705Periplasmic7
Transmembranei706 – 714Beta stranded9
Topological domaini715 – 737ExtracellularAdd BLAST23
Transmembranei738 – 746Beta stranded9
Topological domaini747Periplasmic1

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB02907 2-Amino-Vinyl-Phosphate
DB01814 2-Tridecanoyloxy-Pentadecanoic Acid
DB02700 3-Deoxy-D-Glucosamine
DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid
DB02767 3-Hydroxy-Myristic Acid
DB04039 3-Oxo-Pentadecanoic Acid
DB02379 Beta-D-Glucose
DB02724 Delta-2-Albomycin A1
DB04160 Diphosphate
DB03574 Ferricrocin-Iron
DB03111 Glucosamine 1-Phosphate
DB02865 Glucosamine 4-Phosphate
DB04526 L-Glycero-D-Manno-Heptopyranose
DB03017 Lauric Acid
DB08231 MYRISTIC ACID
DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide
DB02626 Phenylferricrocin-Iron
DB04220 Rifamycin Cgp 4832

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000003474834 – 747Ferrichrome outer membrane transporter/phage receptorAdd BLAST714

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi351 ↔ 362
Disulfide bondi725 ↔ 731

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP06971
PaxDbiP06971
PRIDEiP06971

PTM databases

CarbonylDBiP06971

Expressioni

Inductioni

Induced 1.6-fold by hydroxyurea.1 Publication

Interactioni

Subunit structurei

Monomer (PubMed:8916906, PubMed:9856937, PubMed:9865695). Interacts with TonB (PubMed:9353297, PubMed:12427941, PubMed:18653801).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mcjAQ9X2V72EBI-1116714,EBI-16100378From Escherichia coli.

GO - Molecular functioni

  • protein domain specific binding Source: CAFA

Protein-protein interaction databases

BioGridi4259745139 interactors.
DIPiDIP-9602N
IntActiP06971 6 interactors.
STRINGi316385.ECDH10B_0130

Structurei

Secondary structure

1747
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 46Combined sources3
Helixi55 – 60Combined sources6
Helixi62 – 64Combined sources3
Beta strandi65 – 67Combined sources3
Turni68 – 70Combined sources3
Helixi76 – 78Combined sources3
Beta strandi83 – 87Combined sources5
Helixi88 – 94Combined sources7
Helixi99 – 102Combined sources4
Turni103 – 105Combined sources3
Beta strandi106 – 111Combined sources6
Turni113 – 116Combined sources4
Beta strandi124 – 127Combined sources4
Helixi131 – 133Combined sources3
Beta strandi137 – 139Combined sources3
Helixi156 – 158Combined sources3
Beta strandi159 – 167Combined sources9
Helixi170 – 173Combined sources4
Beta strandi178 – 186Combined sources9
Beta strandi194 – 202Combined sources9
Turni203 – 205Combined sources3
Beta strandi206 – 235Combined sources30
Beta strandi237 – 240Combined sources4
Beta strandi242 – 257Combined sources16
Beta strandi260 – 272Combined sources13
Turni284 – 286Combined sources3
Beta strandi307 – 322Combined sources16
Beta strandi324 – 350Combined sources27
Helixi354 – 356Combined sources3
Helixi360 – 364Combined sources5
Turni367 – 369Combined sources3
Helixi370 – 372Combined sources3
Beta strandi373 – 400Combined sources28
Beta strandi403 – 434Combined sources32
Turni436 – 438Combined sources3
Beta strandi445 – 447Combined sources3
Turni450 – 452Combined sources3
Beta strandi453 – 475Combined sources23
Beta strandi478 – 495Combined sources18
Turni496 – 499Combined sources4
Beta strandi500 – 517Combined sources18
Beta strandi522 – 534Combined sources13
Beta strandi543 – 545Combined sources3
Beta strandi549 – 560Combined sources12
Beta strandi565 – 584Combined sources20
Beta strandi586 – 588Combined sources3
Beta strandi590 – 610Combined sources21
Beta strandi612 – 630Combined sources19
Turni632 – 636Combined sources5
Beta strandi644 – 655Combined sources12
Beta strandi656 – 658Combined sources3
Turni659 – 662Combined sources4
Beta strandi663 – 672Combined sources10
Beta strandi675 – 678Combined sources4
Beta strandi683 – 685Combined sources3
Beta strandi688 – 698Combined sources11
Helixi699 – 702Combined sources4
Beta strandi708 – 715Combined sources8
Beta strandi722 – 727Combined sources6
Beta strandi730 – 733Combined sources4
Beta strandi738 – 746Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BY3X-ray2.74A34-747[»]
1BY5X-ray2.60A34-747[»]
1FCPX-ray2.70A52-747[»]
1FI1X-ray2.90A52-747[»]
1QFFX-ray2.70A34-747[»]
1QFGX-ray2.50A34-747[»]
1QJQX-ray2.95A34-747[»]
1QKCX-ray3.10A34-747[»]
2FCPX-ray2.50A34-747[»]
2GRXX-ray3.30A/B34-747[»]
4CU4X-ray2.30A53-747[»]
ProteinModelPortaliP06971
SMRiP06971
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06971

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni148 – 149Ferrichrome binding3 Publications2
Regioni277 – 279Ferrichrome binding3 Publications3
Regioni346 – 348Ferrichrome binding3 Publications3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi40 – 47TonB box8
Motifi730 – 747TonB C-terminal boxAdd BLAST18

Domaini

Has two distinct conformations in the presence and absence of ferrichrome. The globular N-terminal domain acts a plug that closes the channel formed by the beta-barrel. Binding of ferrichrome at the cell surface induces a conformational change in FhuA, but does not open the channel. Structural changes are propagated and amplified across the plug, and may facilitate binding of FhuA to TonB (PubMed:9865695, PubMed:9353297). TonB binding promotes conformational changes in outer surface-exposed loops of FhuA (PubMed:18653801). Phage T5 is a TonB-independent ligand, and its binding to FhuA results in the formation of high conductance ion channels (PubMed:8617231, PubMed:9353297).4 Publications

Sequence similaritiesi

Belongs to the TonB-dependent receptor family.Curated

Keywords - Domaini

Signal, TonB box, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105E0K Bacteria
COG1629 LUCA
HOGENOMiHOG000260252
InParanoidiP06971
KOiK02014
OMAiFSWRPDD
PhylomeDBiP06971

Family and domain databases

Gene3Di2.170.130.101 hit
2.40.170.201 hit
InterProiView protein in InterPro
IPR012910 Plug_dom
IPR037066 Plug_dom_sf
IPR000531 TonB-dep_rcpt_b-brl
IPR010916 TonB_box_CS
IPR036942 TonB_rcpt_b-brl_sf
IPR010917 TonB_rcpt_CS
IPR010105 TonB_sidphr_rcpt
PfamiView protein in Pfam
PF07715 Plug, 1 hit
PF00593 TonB_dep_Rec, 1 hit
TIGRFAMsiTIGR01783 TonB-siderophor, 1 hit
PROSITEiView protein in PROSITE
PS00430 TONB_DEPENDENT_REC_1, 1 hit
PS01156 TONB_DEPENDENT_REC_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06971-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP
60 70 80 90 100
QESAWGPAAT IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK
110 120 130 140 150
EALSYTPGVS VGTRGASNTY DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN
160 170 180 190 200
DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG LLNMVSKRPT TEPLKEVQFK
210 220 230 240 250
AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG SEEQRYAIAP
260 270 280 290 300
AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN
310 320 330 340 350
EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV
360 370 380 390 400
CSDPANAYSK QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT
410 420 430 440 450
GDIDHTLLTG VDFMRMRNDI NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP
460 470 480 490 500
ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV TLGGRYDWAD QESLNRVAGT
510 520 530 540 550
TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG KDGNIFAPSK
560 570 580 590 600
GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA
610 620 630 640 650
RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW
660 670 680 690 700
ADYTFFDGPL SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA
710 720 730 740
RVGMAGSNVA LHVNNLFDRE YVASCFNTYG CFWGAERQVV ATATFRF
Length:747
Mass (Da):82,182
Last modified:November 1, 1997 - v2
Checksum:i1C2B251D1990E444
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti737R → P in CAA29253 (PubMed:2823072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12486 Genomic DNA Translation: AAB61768.1
U00096 Genomic DNA Translation: AAC73261.1
AP009048 Genomic DNA Translation: BAB96726.2
U70214 Genomic DNA Translation: AAB08580.1
X05810 Genomic DNA Translation: CAA29253.1
PIRiF64738 QRECFE
RefSeqiNP_414692.1, NC_000913.3
WP_000124438.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73261; AAC73261; b0150
BAB96726; BAB96726; BAB96726
GeneIDi944856
KEGGiecj:JW0146
eco:b0150
PATRICifig|1411691.4.peg.2130

Similar proteinsi

Entry informationi

Entry nameiFHUA_ECOLI
AccessioniPrimary (citable) accession number: P06971
Secondary accession number(s): P71280, P75665
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 186 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome